Citation

Georgieva D, Risch M, Kardas A, Buck F, von Bergen M, Betzel C. J. Proteome Res. 2008; 7(3): 866–886.

Affiliation

Institute of Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King Platz 6, 20146 Hamburg, Germany; Institute of Organic Chemistry, Bulgarian Academy of Sciences,“Akad. G. Bonchev”-strasse Bl.9, 1000 Sofia, Bulgaria; Helmholtz-Cent

Copyright

(Copyright © 2008, American Chemical Society)

DOI

10.1021/pr070376c

PMID

18257516

Abstract

The venom proteomics of Vipera ammodytes ammodytes and Vipera ammodytes meridionalis, snakes of public health significance and the most poisonous reptiles in Europe, were analyzed by FPLC, 2-D electrophoresis, sequence analysis, and MS/MS. FPLC analysis showed the presence of l-amino acid oxidase, monomeric and heterodimeric phospholipases A 2, C-type lectin protein, and proteinases in the venom of V. a. ammodytes. Representatives of the same protein families were found in the venom of the other subspecies, V. a. meridionalis. N-terminally identical PLA 2 neurotoxins were identified in both venoms. Difference in the PLA 2 compositions of the venoms was also observed: a monomeric protein with phospholipase A 2 activity, identical in the first 20 amino acid residues to the catalitically inactive acidic component of the heterodimeric PLA 2 present in both venoms, was found only in that of V. a. meridionalis. Probably, this protein represents an intermediate form of the two components of the heterodimer. 2-D electrophoresis and MS/MS analysis showed that the two venoms shared a number of protein families: monomeric and heterodimeric Group II PLA 2s, serine proteinases, Group I, II, and III metalloproteinases, l-amino acid oxidases (LAAOs), cysteine-rich secretory proteins, disintegrins, and growth factors. Totally, 38 venom components of the V. a. ammodytes, belonging to 9 protein families, and 67 components of the V. a. meridionalis venom belonging to 8 protein families were identified. The venom proteome of V. a. ammodytes shows larger diversity of proteins (139) in comparison to that of V. a. meridionalis (104 proteins). Most of the proteins are homologues of known representatives of the respective protein families. The protein compositions explain clinical effects of the V. ammodytes snakebites, such as difficulties in the breathing, paralysis, apoptosis, cloting disorders, hemorrhage, and tissue necrosis. The lists of secreted proteins by the two vipers can be used for further study of structure-function relationships in the toxins and for prediction and treatment of snakebite consequences.

Language: en